Abstract
The signal recognition particle (SRP) recognizes and binds the signal sequence of nascent proteins as they emerge from the ribosome. We present here the 3.0-Å structure of a signal sequence bound to the Methanococcus jannaschii SRP core. Structural comparison with the free SRP core shows that signal-sequence binding induces formation of the GM-linker helix and a 180° flip of the NG domain—structural changes that ensure a hierarchical succession of events during protein targeting.
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Acknowledgements
We thank the European Synchrotron Radiation Facility (Grenoble, France) for provision of synchrotron radiation facilities, and T. Bergfors and U. Sauer for critical reading of the manuscript. This work was supported by the Swedish Research Council (A.E.S.-E.) and Kempe Foundation (A.E.S.-E.).
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T.H., S.H. and A.E.S.-E. contributed to every aspect of this work. G.M. contributed to cloning and protein production and K.B. to Biacore experiments.
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The authors declare no competing financial interests.
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Supplementary Figures 1–7, Supplementary Table 1 and Supplementary Methods (PDF 793 kb)
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Hainzl, T., Huang, S., Meriläinen, G. et al. Structural basis of signal-sequence recognition by the signal recognition particle. Nat Struct Mol Biol 18, 389–391 (2011). https://doi.org/10.1038/nsmb.1994
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DOI: https://doi.org/10.1038/nsmb.1994
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